The structural parameterization of the energetics has been incorporated into a computer program, VDSC, that calculates the expected stability and folding energetics of a monomeric protein from its high resolution structure. All that is required is a file containing the atomic coordinates in the standard PDB format. VDSC calculates the following quantities: 1) Expected heat capacity curve as a function of temperature at the pH specified by the user. 2) Expected heat capacities for the unfolded and native states. 3) Gibbs energy, enthalpy, entropy and heat capacity changes as a function of temperature. 4) Dissection of principal contributions to thermodynamics parameters. 5) Cooperative Interactions. 6) Structural analysis. VDSC allows the user the possibility of treating the protein as a single cooperative unit (two-state unfolding) or to define two different structural domains, thus allowing for an examination of cooperative interactions between structural domains. VDSC is not supposed to replace but to complement experimental differential scanning calorimetry by offering the researcher an opportunity to correlate thermodynamic and structural parameters and to identify features not contemplated in the analysis.